Structural Proteomics Laboratory

 

Institute Biochemistry & Biophysics, Polish Academy of Sciences
Pawińskiego 5a St., 02-106 Warsaw
tel. +48 22 592 34 70-75; e-mail: michald@ibb.waw.pl
Head: Michał Dadlez

 

 

Structural Proteomics Laboratory, IBB PAS (http://mslab-ibb.pl/pl/nanofun) was established in the frame of Mass Spectrometry Laboratory to expand the scope of its activity to protein structure studies. The studies assume application of mass spectrometry methods to obtain unique insight into structural properties of proteins and their assemblies. This is made possible thanks to implementation of new experimental procedures available in new
mass spectrometers, like automated data acquisition and analysis for measurements of hydrogen-deuterium exchange (HDex), ion mobility separation coupled with MS which allows to measure the collisional cross-section or electron transfer dissociation increasing the resolution of HDex measurements. New tools allow to obtain unique structural information especially valuable in the case of difficult protein targets, not yielding to classic methods (crystallography, NMR). These target systems include e.g. oligomerising, natively unfolded or membrane proteins (keratins 8,18, RAGE receptor, Aβ peptide, perfringolysin) that are studied at present.

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Publications based on the research performed in this NanoFun Laboratory:

  1. Aiswarya Premchandar, Norbert Mucke, Jarosław Poznanski, Tatjana Wedig, Magdalena Kaus-Drobek, Harald Herrmann, Michał Dadlez, Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange, THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 291, NO. 48, pp. 24931–24950, November 25, 2016, link
  2. Saša Kazazić, Branimir Bertoša, Marija Luić, Goran Mikleušević, Krzysztof Tarnowski, Michal Dadlez, Marta Narczyk, Agnieszka Bzowska, New Insights into Active Site Conformation Dynamics of E. coli PNP Revealed by Combined H/D Exchange Approach and Molecular Dynamics Simulations, J. Am. Soc. Mass Spectrom. (201 ) 27:73Y82, link
  3. Krzysztof Tarnowski, Kinga Fituch, Roman H. Szczepanowski, Michal Dadlez & Magdalena Kaus-Drobek (2014) Patterns of structural dynamics in RACK1 protein retained throughout evolution: A hydrogen-deuterium exchange study of three orthologs. Protein Science, Volume 23, Issue 5, pages 639–651. link
  4. Ivan Sabath, Aleksandra Skrajna, Xiao-cui Yang, Michał Dadlez, William F. Marzluff and Zbigniew Dominski (2013) 3’ end processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors. RNA, 19, 1726-44, link
  5. Ewa Sitkiewicz, Krzysztof Tarnowski, Jarosław Poznański, Magda Kulma & Michal Dadlez (2013) Oligomerisation interface of RAGE receptor revealed by measurements of hydrogen deuterium exchange monitored by mass spectrometry. PlosOne 8, e76353, link
  6. Yang XC, Sabath I, Dębski J, Kaus-Drobek M, Dadlez M, Marzluff WF, Dominski Z. A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3'-end processing. Mol Cell Biol. 2013 Jan;33(1):28-37. link
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